1dsx: Difference between revisions

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New page: left|200px<br /><applet load="1dsx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dsx, resolution 1.60Å" /> '''KV1.2 T1 DOMAIN, RES...
 
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[[Image:1dsx.gif|left|200px]]<br /><applet load="1dsx" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dsx.gif|left|200px]]<br /><applet load="1dsx" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dsx, resolution 1.60&Aring;" />
caption="1dsx, resolution 1.60&Aring;" />
'''KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT'''<br />
'''KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT'''<br />


==Overview==
==Overview==
Kv voltage-gated potassium channels share a cytoplasmic assembly domain, T1. Recent mutagenesis of two T1 C-terminal loop residues implicates T1 in, channel gating. However, structural alterations of these mutants leave, open the question concerning direct involvement of T1 in gating. We find, in mammalian Kv1.2 that gating depends critically on residues at, complementary T1 surfaces in an unusually polar interface. An isosteric, mutation in this interface causes surprisingly little structural, alteration while stabilizing the closed channel and increasing the, stability of T1 tetramers. Replacing T1 with a tetrameric coiled-coil, destabilizes the closed channel. Together, these data suggest that, structural changes involving the buried polar T1 surfaces play a key role, in the conformational changes leading to channel opening.
Kv voltage-gated potassium channels share a cytoplasmic assembly domain, T1. Recent mutagenesis of two T1 C-terminal loop residues implicates T1 in channel gating. However, structural alterations of these mutants leave open the question concerning direct involvement of T1 in gating. We find in mammalian Kv1.2 that gating depends critically on residues at complementary T1 surfaces in an unusually polar interface. An isosteric mutation in this interface causes surprisingly little structural alteration while stabilizing the closed channel and increasing the stability of T1 tetramers. Replacing T1 with a tetrameric coiled-coil destabilizes the closed channel. Together, these data suggest that structural changes involving the buried polar T1 surfaces play a key role in the conformational changes leading to channel opening.


==About this Structure==
==About this Structure==
1DSX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DSX OCA].  
1DSX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DSX OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Avelar, A.]]
[[Category: Avelar, A.]]
[[Category: Berger, J.M.]]
[[Category: Berger, J M.]]
[[Category: Jan, L.Y.]]
[[Category: Jan, L Y.]]
[[Category: Jan, Y.N.]]
[[Category: Jan, Y N.]]
[[Category: Jr., D.L.Minor.]]
[[Category: Jr., D L.Minor.]]
[[Category: Lin, Y.F.]]
[[Category: Lin, Y F.]]
[[Category: Mobley, B.C.]]
[[Category: Mobley, B C.]]
[[Category: assembly domain]]
[[Category: assembly domain]]
[[Category: tetramer]]
[[Category: tetramer]]
[[Category: voltage-gated potassium channel]]
[[Category: voltage-gated potassium channel]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:33:20 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:06 2008''

Revision as of 13:20, 21 February 2008

File:1dsx.gif


1dsx, resolution 1.60Å

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KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT

OverviewOverview

Kv voltage-gated potassium channels share a cytoplasmic assembly domain, T1. Recent mutagenesis of two T1 C-terminal loop residues implicates T1 in channel gating. However, structural alterations of these mutants leave open the question concerning direct involvement of T1 in gating. We find in mammalian Kv1.2 that gating depends critically on residues at complementary T1 surfaces in an unusually polar interface. An isosteric mutation in this interface causes surprisingly little structural alteration while stabilizing the closed channel and increasing the stability of T1 tetramers. Replacing T1 with a tetrameric coiled-coil destabilizes the closed channel. Together, these data suggest that structural changes involving the buried polar T1 surfaces play a key role in the conformational changes leading to channel opening.

About this StructureAbout this Structure

1DSX is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel., Minor DL, Lin YF, Mobley BC, Avelar A, Jan YN, Jan LY, Berger JM, Cell. 2000 Sep 1;102(5):657-70. PMID:11007484

Page seeded by OCA on Thu Feb 21 12:20:06 2008

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